The objective of this project is to obtain information on the relationship of the structure of blood, milk, and egg white proteins to their physical, chemical, and biological properties. The albumins, riboflavin-binding proteins, freeze point-depressing glycoproteins, and ovomucins will be particularly studied. The comparative approach will be used to study how proteins in general function and, in particular, how homologous proteins of avian eggs, human and bovine milk, and vertebrate blood function. This would be achieved by relating structures of homologous and analogous proteins to their functions and by making further (other than those resulting from genetic differences) changes in structure by chemical modification. Techniques will include physical and chemical characterization, chemical modification, and chemical degradation. BIBLIOGRAPHIC REFERENCES: Tomimatsu, Y., Scherer, J. R., Yeh, Y. and Feeney, R. E., "Raman spectra of a solid antifreeze glycoprotein and its liquid and frozen aqueous solutions" J. Biol. Chem. 251, in press (1976). Ahmed, A. I., Yeh, Y., Osuga, D. T., and Feeney, R. E., "Antifreeze glycoproteins from Antarctic fish. Inactivation by borate" J. Biol. Chem. 251, in press (1976).